Summary for 7AJB
| Entry DOI | 10.2210/pdb7ajb/pdb |
| Related | 6ZPO |
| EMDB information | 11428 |
| Descriptor | ATP synthase protein 8, ATP synthase subunit a, ATP synthase F(0) complex subunit B1, mitochondrial, ... (20 entities in total) |
| Functional Keywords | atp synthase, mitochondria, mammalian, complex, hydrolase |
| Biological source | Bos taurus (Bovine) More |
| Total number of polymer chains | 58 |
| Total formula weight | 1191114.18 |
| Authors | Spikes, T.E.,Montgomery, M.G.,Walker, J.E. (deposition date: 2020-09-29, release date: 2021-02-03, Last modification date: 2021-02-24) |
| Primary citation | Spikes, T.E.,Montgomery, M.G.,Walker, J.E. Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize via interactions between their membrane domains. The dimers form extensive chains along the tips of the cristae with the two rows of monomeric catalytic domains extending into the mitochondrial matrix at an angle to each other. Disruption of the interface between dimers by mutation affects the morphology of the cristae severely. By analysis of particles of purified dimeric bovine ATP synthase by cryo-electron microscopy, we have shown that the angle between the central rotatory axes of the monomeric complexes varies between ca. 76 and 95°. These particles represent active dimeric ATP synthase. Some angular variations arise directly from the catalytic mechanism of the enzyme, and others are independent of catalysis. The monomer-monomer interaction is mediated mainly by j subunits attached to the surface of wedge-shaped protein-lipid structures in the membrane domain of the complex, and the angular variation arises from rotational and translational changes in this interaction, and combinations of both. The structures also suggest how the dimeric ATP synthases might be interacting with each other to form the characteristic rows along the tips of the cristae via other interwedge contacts, molding themselves to the range of oligomeric arrangements observed by tomography of mitochondrial membranes, and at the same time allowing the ATP synthase to operate under the range of physiological conditions that influence the structure of the cristae. PubMed: 33542155DOI: 10.1073/pnas.2021012118 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.2 Å) |
Structure validation
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